Add time:07/20/2019         Source:sciencedirect.com

Publisher SummaryLeupeptin, which is produced by several strains of Streptomyces, has been known as a potent inhibitor for trypsin-family proteases including trypsin, plasmin, kallikrein, and urokinase. One can obtain useful biospecific affinity adsorbents if leupeptin or its essential moiety can be immobilized. To use leupeptin as an immobilized ligand for affinity adsorbents, appropriate modification is required. This chapter develops a new method to expose an a-amino group by using thermolysin. Thermolysin was found to hydrolyze exclusively the leucyl-leucyl bond. The aldehyde group was protected prior to thermolysin digestion and the product was handled under the protected from throughout a series of reaction steps. Finally, the aldehyde group can be regenerated. The adsorbents showed very strong affinity for trypsin-family enzymes. Adsorbed enzymes were bovine and Streptomyces griseus trypsin, plasmin, kallikrein, urokinase, and clostripain. The importance of the aldehyde group of argininal is evident. The Sepharose derivatives adsorbed enzymes only after the acid treatment for removal of the protecting group. The adsorbents completely lost their ability if the aldehyde group was converted to the corresponding alcohol by treatment with NaBH4.

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